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[Proline-specific endopeptidases].

D V Besedin1, G N Rudenskaia

  • 1Chemistry Faculty, Moscow State University, Vorob'evy gory, Moscow, 119899 Russia. laboratoriahps@hotmail.com

Bioorganicheskaia Khimiia
|March 28, 2003
PubMed
Summary
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This review covers prolyl endopeptidases (PEPs), enzymes cleaving after proline residues. It details known PEPs from various organisms and related enzymes, discussing their properties and structures.

Area of Science:

  • Biochemistry
  • Enzymology

Context:

  • Prolyl endopeptidases (PEPs) are crucial enzymes involved in peptide bond hydrolysis.
  • These enzymes specifically cleave peptide substrates at the carbonyl of internal proline (Pro) residues.

Purpose:

  • To review and consolidate current knowledge on prolyl endopeptidases.
  • To discuss the characteristics of known PEPs from diverse biological sources, including animals, microorganisms, fungi, and plants.

Summary:

  • The review encompasses all currently identified prolyl endopeptidases.
  • It also includes post-proline-cleaving enzymes lacking strict proline specificity.
  • Detailed information on physicochemical properties, catalytic mechanisms, substrate specificity, inhibitors, amino acid sequences, and 3D structures is presented.

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Impact:

  • Provides a comprehensive resource for researchers in enzymology and protein science.
  • Facilitates understanding of PEP function and potential applications in biotechnology and medicine.